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Database: UniProt
Entry: A0A1Y4DJU0_9ACTN
LinkDB: A0A1Y4DJU0_9ACTN
Original site: A0A1Y4DJU0_9ACTN 
ID   A0A1Y4DJU0_9ACTN        Unreviewed;       918 AA.
AC   A0A1Y4DJU0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=B5F74_09175 {ECO:0000313|EMBL:OUO58952.1};
OS   Collinsella sp. An271.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=1965616 {ECO:0000313|EMBL:OUO58952.1, ECO:0000313|Proteomes:UP000195889};
RN   [1] {ECO:0000313|Proteomes:UP000195889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An271 {ECO:0000313|Proteomes:UP000195889};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUO58952.1}.
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DR   EMBL; NFJE01000010; OUO58952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4DJU0; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000195889; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195889};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..266
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          676..882
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   918 AA;  100001 MW;  C5840AEBF25F24B7 CRC64;
     MPDTRRTFAV IDGNSLMHRA FHAVPPTMNA PDGRPTNAIF GFLNMFLKMI DAFHPDGVAV
     AFDRGKPRVR MEMLPQYKAQ RPPMDPDLRQ QFPMIKELLS KLSVPILEAE GWEGDDILGT
     LARTGEAAGC DMYLITGDRD MYQLSTEHVK IVGTKKGLSD VQIMTPESVE DLYHGITPEL
     VPDFYGLKGD TSDNIPGVPG IGPKKASALI AQYGSLDEVI AHADEVKGKM GENLRAHIDD
     ALLSRKVATI QTNAPVELDF EHTAFPAYDA SSVADALGEL GINAMQNRFL ALIGGEGAPE
     AAASTLDIPD ALHAYAATGE DVEQAARELA RAIEAGEWIA AVLDDDREAG ALFGLTHTLW
     VAAPDALLAF EEPDGGACDL PKVDGYDFSH GLIAGVLLRL FGEGKVVSPD VKALIHELAP
     ADSSVPAHID ALAIDPDRIF DTVVAAYLLD SARSSFDDGY IADAYLNVQL PAAAGEDGAA
     EGAVPAAARS AVLARTALMP LAESLDRQGA ARVFTQIEMP LIPVLADMER TGMRLDPERL
     SEMSDKLVGQ IDELAGRIRA LAGDDSFNIA SPMQLSHILF DVMGLPTKGL KKTQRGYYST
     NAKVLDDLAR DHEIVRLILE WREKTKIKST YLDTLGQQRR GDGRVHTTYN QTITATGRLS
     SSNPNLQNIP TRSELGHTVK TAFAAGEGAV FLAVDYSQIE LRLLAHLSED EHLVRAFNEG
     EDFHAETAAR VFGVPVEEVT PQLRSRAKAV NFGIVYGQQA YGLSQSLDIP MAEAREMIEA
     YFRAYPGVRT YLDRTVAEAK RTGYAETMFG RRRPIPELKM RNPAQRSFGE RTAMNHPMQG
     SAADIIKIAM ARVARRLHDE GFAARMILQV HDELDFECPV DEVERLTAMV VEEMEGVVKL
     RVPLIAEAST GVTWADAK
//
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